SURE_SALTY
ID SURE_SALTY Reviewed; 253 AA.
AC P66881; Q8XFG4;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=5'/3'-nucleotidase SurE {ECO:0000255|HAMAP-Rule:MF_00060};
DE EC=3.1.3.5 {ECO:0000255|HAMAP-Rule:MF_00060};
DE EC=3.1.3.6 {ECO:0000255|HAMAP-Rule:MF_00060};
DE AltName: Full=Exopolyphosphatase {ECO:0000255|HAMAP-Rule:MF_00060};
DE EC=3.6.1.11 {ECO:0000255|HAMAP-Rule:MF_00060};
DE AltName: Full=Nucleoside monophosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00060};
GN Name=surE {ECO:0000255|HAMAP-Rule:MF_00060}; OrderedLocusNames=STM2927;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Nucleotidase with a broad substrate specificity as it can
CC dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates
CC and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP.
CC Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the
CC preference for short-chain-length substrates (P20-25). Might be
CC involved in the regulation of dNTP and NTP pools, and in the turnover
CC of 3'-mononucleotides produced by numerous intracellular RNases (T1,
CC T2, and F) during the degradation of various RNAs. {ECO:0000255|HAMAP-
CC Rule:MF_00060}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00060};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 3'-phosphate + H2O = a ribonucleoside +
CC phosphate; Xref=Rhea:RHEA:10144, ChEBI:CHEBI:13197,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474; EC=3.1.3.6;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00060};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphate](n) + H2O = [phosphate](n-1) + H(+) + phosphate;
CC Xref=Rhea:RHEA:21528, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14279,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16838,
CC ChEBI:CHEBI:43474; EC=3.6.1.11; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00060};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00060};
CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00060};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00060}.
CC -!- SIMILARITY: Belongs to the SurE nucleotidase family.
CC {ECO:0000255|HAMAP-Rule:MF_00060}.
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DR EMBL; AE006468; AAL21807.1; -; Genomic_DNA.
DR RefSeq; NP_461848.1; NC_003197.2.
DR RefSeq; WP_001221538.1; NC_003197.2.
DR PDB; 2V4N; X-ray; 1.70 A; A=1-253.
DR PDB; 2V4O; X-ray; 2.71 A; A/B/C/D=1-253.
DR PDB; 4G9O; X-ray; 2.12 A; A/B=1-253.
DR PDB; 4GAD; X-ray; 2.35 A; A/B=1-253.
DR PDB; 4RYT; X-ray; 2.09 A; A=1-253.
DR PDB; 4RYU; X-ray; 2.04 A; A/B/C/D=1-253.
DR PDB; 4XEP; X-ray; 1.50 A; A=1-253.
DR PDB; 4XER; X-ray; 1.97 A; A/B/C/D=1-253.
DR PDB; 4XGB; X-ray; 2.23 A; A/B/C/D=1-253.
DR PDB; 4XGP; X-ray; 1.90 A; A/B/C/D=1-253.
DR PDB; 4XH8; X-ray; 3.56 A; A/B=1-253.
DR PDB; 4XJ7; X-ray; 1.60 A; A/B/C/D=1-253.
DR PDBsum; 2V4N; -.
DR PDBsum; 2V4O; -.
DR PDBsum; 4G9O; -.
DR PDBsum; 4GAD; -.
DR PDBsum; 4RYT; -.
DR PDBsum; 4RYU; -.
DR PDBsum; 4XEP; -.
DR PDBsum; 4XER; -.
DR PDBsum; 4XGB; -.
DR PDBsum; 4XGP; -.
DR PDBsum; 4XH8; -.
DR PDBsum; 4XJ7; -.
DR AlphaFoldDB; P66881; -.
DR SMR; P66881; -.
DR STRING; 99287.STM2927; -.
DR PaxDb; P66881; -.
DR EnsemblBacteria; AAL21807; AAL21807; STM2927.
DR GeneID; 1254450; -.
DR KEGG; stm:STM2927; -.
DR PATRIC; fig|99287.12.peg.3081; -.
DR HOGENOM; CLU_045192_1_2_6; -.
DR OMA; DCVHIAL; -.
DR PhylomeDB; P66881; -.
DR BioCyc; SENT99287:STM2927-MON; -.
DR EvolutionaryTrace; P66881; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008254; F:3'-nucleotidase activity; IBA:GO_Central.
DR GO; GO:0008253; F:5'-nucleotidase activity; IBA:GO_Central.
DR GO; GO:0004309; F:exopolyphosphatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046050; P:UMP catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.1210.10; -; 1.
DR HAMAP; MF_00060; SurE; 1.
DR InterPro; IPR030048; SurE.
DR InterPro; IPR002828; SurE-like_Pase/nucleotidase.
DR InterPro; IPR036523; SurE-like_sf.
DR PANTHER; PTHR30457; PTHR30457; 1.
DR Pfam; PF01975; SurE; 1.
DR SUPFAM; SSF64167; SSF64167; 1.
DR TIGRFAMs; TIGR00087; surE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..253
FT /note="5'/3'-nucleotidase SurE"
FT /id="PRO_0000111839"
FT BINDING 8
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT BINDING 9
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT BINDING 39
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT BINDING 92
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:4XEP"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:4XEP"
FT STRAND 27..36
FT /evidence="ECO:0007829|PDB:4XEP"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:4XEP"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:4XEP"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:4XEP"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2V4N"
FT STRAND 85..94
FT /evidence="ECO:0007829|PDB:4XEP"
FT HELIX 98..103
FT /evidence="ECO:0007829|PDB:4XEP"
FT HELIX 105..111
FT /evidence="ECO:0007829|PDB:4XEP"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:4XEP"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:4XEP"
FT STRAND 120..129
FT /evidence="ECO:0007829|PDB:4XEP"
FT HELIX 131..147
FT /evidence="ECO:0007829|PDB:4XEP"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:4XEP"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:4XEP"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:4XEP"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:2V4N"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:4XEP"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:4XEP"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:4XEP"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:4XEP"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:4XEP"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:4XEP"
FT HELIX 237..247
FT /evidence="ECO:0007829|PDB:4XEP"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:4XJ7"
SQ SEQUENCE 253 AA; 26980 MW; A8C4DD6EE42372F8 CRC64;
MRILLSNDDG VHAPGIQTLA KALREFADVQ VVAPDRNRSG ASNSLTLESS LRTFTFDNGD
IAVQMGTPTD CVYLGVNALM RPRPDIVVSG INAGPNLGDD VIYSGTVAAA MEGRHLGFPA
LAVSLNGYQH YDTAAAVTCA LLRGLSREPL RTGRILNVNV PDLPLAQVKG IRVTRCGSRH
PADKVIPQED PRGNTLYWIG PPGDKYDAGP DTDFAAVDEG YVSVTPLHVD LTAHSAHDVV
SDWLDSVGVG TQW
